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1 October 2004 FUNCTIONAL CHARACTERIZATION OF AN LCCL–LECTIN DOMAIN CONTAINING PROTEIN FAMILY IN PLASMODIUM BERGHEI
Holly E. Trueman, J. Dale Raine, Laurence Florens, Johannes T. Dessens, Jacqui Mendoza, Jeffrey Johnson, Cecilia C. Waller, Isabelle Delrieu, Anthony A. Holder, Jean Langhorne, Daniel J. Carucci, John R. Yates, Robert E. Sinden
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Abstract

Using bioinformatic, proteomic, immunofluorescence, and genetic cross methods, we have functionally characterized a family of putative parasite ligands as potential mediators of cell–cell interactions. We name these proteins the Limulus clotting factor C, Coch-5b2, and Lgl1 (LCCL)–lectin adhesive–like protein (LAP) family. We demonstrate that this family is conserved amongst Plasmodium spp. It possesses a unique arrangement of adhesive protein domains normally associated with extracellular proteins. The proteins are expressed predominantly, though not exclusively, in the mosquito stages of the life cycle. We test the hypothesis that these proteins are surface proteins with 1 member of this gene family, lap1, and provide evidence that it is expressed on the surface of Plasmodium berghei sporozoites. Finally, through genetic crosses of wild-type Pblap1 and transgenic Pblap1 parasites, we show that the null phenotype previously reported for sporozoite development in a Pblap1 mutant can be rescued within a heterokaryotic oocyst and that infectious Pblap1 sporozoites can be formed. The mutant is not rescued by coparasitization of mosquitoes with a mixture Pblap1 and Pblap1 homokaryotic oocysts.

Holly E. Trueman, J. Dale Raine, Laurence Florens, Johannes T. Dessens, Jacqui Mendoza, Jeffrey Johnson, Cecilia C. Waller, Isabelle Delrieu, Anthony A. Holder, Jean Langhorne, Daniel J. Carucci, John R. Yates, and Robert E. Sinden "FUNCTIONAL CHARACTERIZATION OF AN LCCL–LECTIN DOMAIN CONTAINING PROTEIN FAMILY IN PLASMODIUM BERGHEI," Journal of Parasitology 90(5), 1062-1071, (1 October 2004). https://doi.org/10.1645/GE-3368
Received: 15 December 2003; Accepted: 1 February 2004; Published: 1 October 2004
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